Mammalian heme peroxidases are fascinating due to their unique peculiarity of oxidizing
(pseudo)halides under physiologically relevant conditions. These proteins are able either to incorporate oxidized halides into substrates adjacent to the active site or to generate different oxidized
(pseudo)halogenated species, which can take part in multiple (pseudo)halogenation and oxidation
reactions with cell and tissue constituents. The present article reviews basic biochemical and redox
mechanisms of (pseudo)halogenation activity as well as the physiological role of heme peroxidases.
Thyroid peroxidase and peroxidasin are key enzymes for thyroid hormone synthesis and the formation of functional cross-links in collagen IV during basement membrane formation. Special attention
is directed to the properties, enzymatic mechanisms, and resulting (pseudo)halogenated products of
the immunologically relevant proteins such as myeloperoxidase, eosinophil peroxidase, and lactoperoxidase. The potential role of the (pseudo)halogenated products (hypochlorous acid, hypobromous
acid, hypothiocyanite, and cyanate) of these three heme peroxidases is further discussed
| Identifer | oai:union.ndltd.org:DRESDEN/oai:qucosa:de:qucosa:85913 |
| Date | 09 June 2023 |
| Creators | Arnhold, Jürgen, Malle, Ernst |
| Publisher | MDPI |
| Source Sets | Hochschulschriftenserver (HSSS) der SLUB Dresden |
| Language | English |
| Detected Language | English |
| Type | info:eu-repo/semantics/publishedVersion, doc-type:article, info:eu-repo/semantics/article, doc-type:Text |
| Rights | info:eu-repo/semantics/openAccess |
| Relation | 890 |
Page generated in 0.0019 seconds